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Conserved domains on  [gi|627899741|ref|XP_007690593|]
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uncharacterized protein COCMIDRAFT_28563 [Bipolaris oryzae ATCC 44560]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PFM_aerolysin-like cd20242
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 177-317 2.23e-66

pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized subgroup; Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


:

Pssm-ID: 380812 [Multi-domain]  Cd Length: 144  Bit Score: 204.96  E-value: 2.23e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 177 PVNIHSQEATNDTSEPQTPLIEVLKTTEQQYTFESEVGLELGISTKFSSGIPVAAKAEVKISAKIHTNLSWGIANSHSQT 256
Cdd:cd20242    1 PASLYSQTVTNDTGQPQTPSISGSETVTETSTWEDEVGLKLGVSTSFSAGVPVVAEGKVEVSAEVHNNYTWNGSNTRSKT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 627899741 257 WKSSVPLNVPGHKTYKVTMTVTEYTIRVPFKAKWKSP---ATKKTIVTEGVFKGINSSELKTNY 317
Cdd:cd20242   81 WSFSTPVNVPAHSAVRATATVTESTISVPYTLTWKSIfesGARVTGTIEGMYKGSNSHDLTTNF 144
beta-trefoil_Ricin-like super family cl49609
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 7-154 4.79e-33

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats.


The actual alignment was detected with superfamily member cd23424:

Pssm-ID: 483949  Cd Length: 144  Bit Score: 119.38  E-value: 4.79e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741   7 IPSPDLRVRIINTESRLALYSNARDKLGLNHVDISIPYRDQYWYVRPGQGKNAGLYLIVSDYNDRAIYVDFENGLQwgpA 86
Cdd:cd23424    1 IPPPGLRFRLLGYASQQVIFSRTSNSPRVGHSPSSEVYDDQYFTLIPGTGPHAGLYAIKSKATGKVIFSRRGASPQ---V 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 627899741  87 GTSAPAGSSDLQYFDLaqQQGKGIRAGQFRIYNPTNDGVLFSRTNQQYEIGCVSNAMGTFNDQWFTFE 154
Cdd:cd23424   78 GSIDGDGSYDDQWFKF--EPGKGDFKGYFRLVNPATDTVLFSRTTLEPQFGNIPADQPVFDDQYFSFL 143
 
Name Accession Description Interval E-value
PFM_aerolysin-like cd20242
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 177-317 2.23e-66

pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized subgroup; Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380812 [Multi-domain]  Cd Length: 144  Bit Score: 204.96  E-value: 2.23e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 177 PVNIHSQEATNDTSEPQTPLIEVLKTTEQQYTFESEVGLELGISTKFSSGIPVAAKAEVKISAKIHTNLSWGIANSHSQT 256
Cdd:cd20242    1 PASLYSQTVTNDTGQPQTPSISGSETVTETSTWEDEVGLKLGVSTSFSAGVPVVAEGKVEVSAEVHNNYTWNGSNTRSKT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 627899741 257 WKSSVPLNVPGHKTYKVTMTVTEYTIRVPFKAKWKSP---ATKKTIVTEGVFKGINSSELKTNY 317
Cdd:cd20242   81 WSFSTPVNVPAHSAVRATATVTESTISVPYTLTWKSIfesGARVTGTIEGMYKGSNSHDLTTNF 144
beta-trefoil_Ricin_BEL-like cd23424
ricin B-type lectin domain, beta-trefoil fold, found in Boletus edulis lectin (BEL), ...
 7-154 4.79e-33

ricin B-type lectin domain, beta-trefoil fold, found in Boletus edulis lectin (BEL), Laetiporus sulphureus lectin (LSL) and similar proteins; BEL has potent anti-proliferative effects on human cancer cells. It functions as a homodimer and each protomer folds as a beta-trefoil. The BEL beta-trefoil binds galactose and other galactose-containing carbohydrates. LSL is a lectin that exhibits hemolytic and hemagglutinating activities. It functions as a hexamer. Its monomeric protein consists of two distinct modules: an N-terminal beta-trefoil lectin module (LSL150) and a C-terminal membrane pore-forming module (PFM). All members of this subfamily contain a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (called alpha, beta, and gamma, respectively) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding site. Due to the lack of an aromatic residue, the sugar binding within alpha-site of LSL150 might be absent.


Pssm-ID: 467302  Cd Length: 144  Bit Score: 119.38  E-value: 4.79e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741   7 IPSPDLRVRIINTESRLALYSNARDKLGLNHVDISIPYRDQYWYVRPGQGKNAGLYLIVSDYNDRAIYVDFENGLQwgpA 86
Cdd:cd23424    1 IPPPGLRFRLLGYASQQVIFSRTSNSPRVGHSPSSEVYDDQYFTLIPGTGPHAGLYAIKSKATGKVIFSRRGASPQ---V 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 627899741  87 GTSAPAGSSDLQYFDLaqQQGKGIRAGQFRIYNPTNDGVLFSRTNQQYEIGCVSNAMGTFNDQWFTFE 154
Cdd:cd23424   78 GSIDGDGSYDDQWFKF--EPGKGDFKGYFRLVNPATDTVLFSRTTLEPQFGNIPADQPVFDDQYFSFL 143
Aerolysin pfam01117
Aerolysin toxin; This family represents the pore forming lobe of aerolysin.
 151-289 3.54e-04

Aerolysin toxin; This family represents the pore forming lobe of aerolysin.


Pssm-ID: 366474  Cd Length: 359  Bit Score: 41.86  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741  151 FTFEAEPLELIniefdLKNTVTESVRPVNIHSQEATNDTSEPQTPLIEVLKTTEQQYTFESEVGLELGISTKFSSGIPva 230
Cdd:pfam01117  80 FKFGVKPSSLK-----YGDPVISDREPYKYIVGYARNDSDTPQQRVLTLSYDEVTNWSKTDTYKYSEKVTIKNKYKFP-- 152

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 627899741  231 AKAEVKISAKIHTNLSWGIANSHSQTW--KSSVPLNVPGHKTYKVTMTVTEYTIRVPFKAK 289
Cdd:pfam01117 153 LIGETELSLELGANQSWATTNGNSSTKtiSDVARVLVPANTKIPVRLKLEKARVDYPYEFN 213
 
Name Accession Description Interval E-value
PFM_aerolysin-like cd20242
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 177-317 2.23e-66

pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized subgroup; Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380812 [Multi-domain]  Cd Length: 144  Bit Score: 204.96  E-value: 2.23e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 177 PVNIHSQEATNDTSEPQTPLIEVLKTTEQQYTFESEVGLELGISTKFSSGIPVAAKAEVKISAKIHTNLSWGIANSHSQT 256
Cdd:cd20242    1 PASLYSQTVTNDTGQPQTPSISGSETVTETSTWEDEVGLKLGVSTSFSAGVPVVAEGKVEVSAEVHNNYTWNGSNTRSKT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 627899741 257 WKSSVPLNVPGHKTYKVTMTVTEYTIRVPFKAKWKSP---ATKKTIVTEGVFKGINSSELKTNY 317
Cdd:cd20242   81 WSFSTPVNVPAHSAVRATATVTESTISVPYTLTWKSIfesGARVTGTIEGMYKGSNSHDLTTNF 144
beta-trefoil_Ricin_BEL-like cd23424
ricin B-type lectin domain, beta-trefoil fold, found in Boletus edulis lectin (BEL), ...
 7-154 4.79e-33

ricin B-type lectin domain, beta-trefoil fold, found in Boletus edulis lectin (BEL), Laetiporus sulphureus lectin (LSL) and similar proteins; BEL has potent anti-proliferative effects on human cancer cells. It functions as a homodimer and each protomer folds as a beta-trefoil. The BEL beta-trefoil binds galactose and other galactose-containing carbohydrates. LSL is a lectin that exhibits hemolytic and hemagglutinating activities. It functions as a hexamer. Its monomeric protein consists of two distinct modules: an N-terminal beta-trefoil lectin module (LSL150) and a C-terminal membrane pore-forming module (PFM). All members of this subfamily contain a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (called alpha, beta, and gamma, respectively) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding site. Due to the lack of an aromatic residue, the sugar binding within alpha-site of LSL150 might be absent.


Pssm-ID: 467302  Cd Length: 144  Bit Score: 119.38  E-value: 4.79e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741   7 IPSPDLRVRIINTESRLALYSNARDKLGLNHVDISIPYRDQYWYVRPGQGKNAGLYLIVSDYNDRAIYVDFENGLQwgpA 86
Cdd:cd23424    1 IPPPGLRFRLLGYASQQVIFSRTSNSPRVGHSPSSEVYDDQYFTLIPGTGPHAGLYAIKSKATGKVIFSRRGASPQ---V 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 627899741  87 GTSAPAGSSDLQYFDLaqQQGKGIRAGQFRIYNPTNDGVLFSRTNQQYEIGCVSNAMGTFNDQWFTFE 154
Cdd:cd23424   78 GSIDGDGSYDDQWFKF--EPGKGDFKGYFRLVNPATDTVLFSRTTLEPQFGNIPADQPVFDDQYFSFL 143
PFM_LSL-like cd20215
pore-forming module of Laetiporus sulphureus LSL lectin and similar aerolysin-type beta-barrel ...
 156-317 5.72e-30

pore-forming module of Laetiporus sulphureus LSL lectin and similar aerolysin-type beta-barrel pore-forming proteins; LSL is a lectin, produced by the parasitic mushroom Laetiporus sulphureus, which exhibits hemolytic and hemagglutinating activities. Members of this family belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380785 [Multi-domain]  Cd Length: 164  Bit Score: 111.65  E-value: 5.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 156 EPLELINIEFDLKNTVTESVRPVNIHSQEATNDTSEPQTPLIEVLKTTEQQYTFESEVGLELGISTKFSSGIPVAAKAEV 235
Cdd:cd20215    1 EDMEIVSVEYDLDKGKILSSTPLVLARQTLRNDTDVEQTMSFTLTETETHTSTFEYTAGFTITVGTSFKAGIPGVAEGKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 236 KISAKIHTNLSWGIANSHSQTWKSSVPLNVPGHKTYKVTMTVTEYTIRVPFKAKWKSPATKKTIVTEGVFKGINSSELKT 315
Cdd:cd20215   81 KVDTTVSNEWKWGESTTFTKTYTATFPVKAPPGSTVRAVATVTKSNLEVPFTMTLKSKSTGYEVETKGIYRGVSTWNLRT 160


                 ..
gi 627899741 316 NY 317
Cdd:cd20215  161 AI 162
PFM_aerolysin-like cd20241
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 183-307 8.05e-19

pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized subgroup; Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380811 [Multi-domain]  Cd Length: 139  Bit Score: 81.38  E-value: 8.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 183 QEATNDTSEPQTPLIEVLKTTEQQYTFESEVGLELGISTKFSSGIPVAAKAEVKISAKIHTNLSWGIANSHSQTWKSSVP 262
Cdd:cd20241    6 VTVRNNGNTPATLKANMSRSVSETGSFSFTHGFSIGVGTTIKAGIPFIVEGEIETELSTSHDFTWGKSTTVTTTVGSSVT 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 627899741 263 LNVPGHKTYKVTMTVTEYTIRVPFKAKWKSPATKKTIVTEGVFKG 307
Cdd:cd20241   86 VEVPPRSTQTVVGTFKRSKMTVPAKIYSKSKSTGVEVITEAVYRG 130
PFM_HFR-2-like cd20216
pore-forming module of wheat HFR-2 toxin, FEM32, and similar aerolysin-type beta-barrel ...
 176-316 1.45e-15

pore-forming module of wheat HFR-2 toxin, FEM32, and similar aerolysin-type beta-barrel pore-forming proteins; HFR-2 is a wheat cytolytic toxin which may normally function in defense against certain insects or pathogens. The Hfr-2 gene is upregulated in virulent Hessian fly larval feedingdouble dagger. The HFR-2 protein may insert in plant cell membranes at the feeding sites and by forming pores provide water, ions and other small nutritive molecules to the developing larvae. This group also contains FEM32, a flower-specific lectin-like protein from the dioecious plant Rumex acetosa, which alters flower development and induces male sterility in transgenic tobacco. It has been suggested that the FEM32 gene activates some form of programmed cell death (PCD), a process that could be mediated by the action of its lectin domains for binding to specific glycoproteins on the cell membrane and facilitated by the formation of pore structures in the membranes and the subsequent leakage of the cytosolic content through its pore-forming aerolysin domain. Most proteins belonging to this group have N-terminal agglutatin (also known as amaranthin) lectin domains; most have two agglutatin domains, in combination with one aerolysin domain. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380786 [Multi-domain]  Cd Length: 152  Bit Score: 72.62  E-value: 1.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 176 RPVNIHSQEATNDTSEPQTPLIEVLKTTEQQYTFESEVGLELGISTKFSSGIPVAAKAEVKISAKIHTNLSWGIANSHSQ 255
Cdd:cd20216    5 KVLTLATGEATNNTSEPQTVTLKLSYTDTKTSTWNSSVSLKLGVKTTISAGVPFIVDGKIEISAEFSGSYEWGETKTETT 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 256 TWKSSVPLNVPGHKTYKVTMTVTEYTIRVPFkakwkS------PATKKTIVTE---GVFKGINSSELKTN 316
Cdd:cd20216   85 EVETTYTVTVPPMTKVTVTLIATRGSCDVPF-----SytqrdtLTNGTTVTYEkddGLYTGVNSYNFKYE 149
PFM_natterin-3-like cd20220
pore-forming module of Thalassophryne nattereri fish venom natterins 1-4, and similar ...
 177-315 9.52e-14

pore-forming module of Thalassophryne nattereri fish venom natterins 1-4, and similar aerolysin-type beta-barrel pore-forming proteins; This group includes 4 of the 5 Thalassophryne nattereri fish venom natterins: natterin-1, -2, -3, and 4. Natterins have kininogenase activity, kallikrein activity, and are allodynic and edema inducing. They also cleave type I and type IV collagen, resulting in necrosis of the affected cells. Contradictory to their edematic activity, Natterins also have anti-inflammatory effects through inhibition of interactions between leukocytes and the endothelium, and reduction in neutrophil accumulation. Many proteins belonging to this group have an N-terminal DUF3421 domain. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380790 [Multi-domain]  Cd Length: 152  Bit Score: 67.65  E-value: 9.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 177 PVNIHSQEATNDTSEP--QTPLIEvlKTTEQQYTFESEVGLELGISTKFSSGIPVAAKAEVKISAKIHTNLSWGIANSHS 254
Cdd:cd20220    6 PETLKESTVTNNGCKPvkKTVTLS--KTTEVEHRWDTSFSITLGVSTTITAGIPIIAGGGWEVSTETTFTWSGGTSVTES 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 627899741 255 QTWKSSVPLNVPGHKTYKVTMTVTEYTIRVPFKAK----WKSPATKKTIVTeGVFKGINSSELKT 315
Cdd:cd20220   84 VTHSVSVEVTVPPNHSCTVKMVGYKYKADIPFTARltrtYRNGETHTTTIT-GTYKGVQVGEVRA 147
PFM_Dln1-like cd20221
pore-forming module of Danio rerio Dln1, and similar aerolysin-type beta-barrel pore-forming ...
 159-316 2.44e-12

pore-forming module of Danio rerio Dln1, and similar aerolysin-type beta-barrel pore-forming proteins; Since Danio rerio Dln1 has a specific affinity towards high-mannose glycans, which are common on the surface of virus and fungi, it has been suggested that it may play a defense role. Members of this group also include lamprey immune protein (LIP), a defense molecule derived from lamprey supraneural body tissue which has efficient cytocidal actions against tumor cells. Many proteins belonging to this group have a N-terminal Jacalin-like lectin domain. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380791 [Multi-domain]  Cd Length: 168  Bit Score: 64.31  E-value: 2.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 159 ELINIEFDLKNTVTESVRPVNIHSQEATNDTSEPQTPLIEVLKTTEQQYTFESEVGLELGISTKFSSGIPVAAKAEVKIS 238
Cdd:cd20221    4 VLTNVNYPTLHQVIPQVAVEEIKSMSYENDTSVPQEYTIETSKKITKTSSWSVTNKLESTFSVEVSAGIPEVVEVSTGFS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 239 AKIHTNLSWGIANSHSQTWKSSVPLNVPGHKTYKVTMTVTEYTIRVPFKAKWK----SPATKKtIVTEGVFKGINSSELK 314
Cdd:cd20221   84 LTVGVESTHSLENTEEKTETLSFPVKVPPGKTVDVEITIGRATVDLPYTGTVKitcyNGSVLK-FPTSGIYKGVTYTDAK 162


                 ..
gi 627899741 315 TN 316
Cdd:cd20221  163 VV 164
PFM_aerolysin-like cd20239
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 177-310 2.45e-12

pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized subgroup; Generally, pore-forming proteins (PFPs) are secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores detrimental to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel. Many of this family are bacterial toxins. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380809 [Multi-domain]  Cd Length: 145  Bit Score: 63.63  E-value: 2.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 177 PVNIHSQEATNDTSEP--QTPLIEVLKTTEQqyTFESEVGLELGISTKFSSGIPVAAKAEVKISAKIHTNLSWGIANSHS 254
Cdd:cd20239    1 PTVALSTVVRNDSDSPasQTLTYSYSKSEEG--TWNNTAGIELGVKVTFKAGVPFVASGELEVSVSASYSHTWGGSTTVT 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 627899741 255 QTWKSSVPLNVPGHKTYKVTMTVTEYTIRVPFKAKWKSPATKKTI---VTEGVFKGINS 310
Cdd:cd20239   79 KTVSSSTTVVVPPRKKGVASVLIRKAEIDVPFTYTERITYTGGRMeeeVKTGIYHNVDS 137
PFM_aerolysin-like cd20240
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 174-317 2.89e-12

pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized subgroup; Generally, pore-forming proteins (PFPs) are secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores detrimental to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel. Many of this family are bacterial toxins. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380810 [Multi-domain]  Cd Length: 145  Bit Score: 63.44  E-value: 2.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 174 SVRPVNIHSQEATNDTSEPQTPLIEVLKTTEQQYTFESEVGLELGISTKFSSGIPVAAKAEVKISAKIHTNLSWGIANSH 253
Cdd:cd20240    2 SEIPDFIVTWTYTNNTSIEQTMTTNFSETATETSSFSETEGVSTTVSTSLKVGIPFIAGGEITTTTTTSQSWTYGKSETK 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 627899741 254 SQTWKSSVPLNVPGHKTYKVTMTVTEYTIRVPFKAKWKSPATKKTIVTEGVFKGINSSELKTNY 317
Cdd:cd20240   82 TDTISYTFPIVVPPNTTVTATAVVTKYNMDVTYVATLRGINTGKRIKIKGKWSGVDCTDISYNL 145
PFM_epsilon-toxin-like cd20223
pore-forming module of Clostridium perfringens epsilon-toxin and similar aerolysin-type ...
 168-282 1.54e-11

pore-forming module of Clostridium perfringens epsilon-toxin and similar aerolysin-type beta-barrel pore-forming proteins; Clostridium perfringens epsilon-toxin is responsible for fatal enterotoxemia in ungulates. It forms a heptamer in the lipid rafts of Madin-Darby Canine Kidney (MDCK) cells, leading to cell death; its oligomer formation is induced by activation of neutral sphingomyelinase. This group also includes an insecticidal crystal protein Cry14-4 (encoded on plasmid pBMBt1 of Bacillus thuringiensis serovar darmstadiensis). Also included is pXO2-60 (a protein from the pathogenic pXO2 plasmid of Bacillus anthracis) which harbors a unique ubiquitin-like fold domain at the C-terminus of the aerolysin-like domain, and is involved in virulence. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380793 [Multi-domain]  Cd Length: 144  Bit Score: 61.09  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 168 KNTVTESVRPVNIHSQEATNDTSEPQTplievLKTTEQQYTFESEV------GLELGISTKFSSGIPVAAKAEVKISAKI 241
Cdd:cd20223    5 GDPKITNGEPLYVGSNTLTNDTDEEQT-----LKTPSFSKTVTDTVtttttnGFKLGVSTSAKFKIPFPGGGSTELSAEY 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 627899741 242 HTNLSWGIANSHSQTWKS-SVPLNVPGHKTYKVTMTVTEYTI 282
Cdd:cd20223   80 NFSTTNTNTTSETKTYTApSQTIKVPPGKTYKVTVYLKKVKF 121
PFM_LIN24-like cd20237
pore-forming module of Caenorhabditis elegans LIN-24 and similar aerolysin-type beta-barrel ...
 176-279 1.48e-08

pore-forming module of Caenorhabditis elegans LIN-24 and similar aerolysin-type beta-barrel pore-forming proteins; The process of cytotoxic cell death occurs in Caenorhabditis elegans containing mutations in either of lin-24 and lin-33. The cytotoxicity caused by mutation of either gene requires the function of the other. Genes required for the engulfment of apoptotic corpses function in the cytotoxic cell deaths induced by mutations in lin-24 and lin-33. It has been proposed that Caenorhabditis elegans LIN-24 may function to interact with bacterial toxins having similarity with it, and inactivate these, thereby allowing C. elegans to consume or survive exposure to bacteria that produce such toxins. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380807  Cd Length: 120  Bit Score: 52.19  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 176 RPVNIHSQEATNDTSEPQTPLIEVLKTTEQQYTFESEVGLELGISTKFSSGIP-VAAKAEVKISAKIHTNLSWGIANSHS 254
Cdd:cd20237    1 KSVVLFKTTFTNNTSTEQEYTFKTERTTTSSCTWSVTEGFTIGGEVSLKLGPPpDIAEANAGFSRELSLSKTQEETFEEE 80

                         90       100
                 ....*....|....*....|....*
gi 627899741 255 QTWKSSVPLNVPGHKTYKVTMTVTE 279
Cdd:cd20237   81 LTWSVDSQVTVPPKTKVTAELVITE 105
PFM_aerolysin_family cd10140
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; Pore-forming proteins ...
 254-323 6.51e-08

pore-forming module of aerolysin-type beta-barrel pore-forming proteins; Pore-forming proteins (PFPs) are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta pore-forming proteins (beta-PFPs) form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Members of this family includes enterolobin, a cytolytic, inflammatory and insecticidal protein from the Brazilian tree Enterolobium contortisiliquum.


Pssm-ID: 380782  Cd Length: 92  Bit Score: 49.47  E-value: 6.51e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 254 SQTWKSSVPLNVPGHKTYKVTMTVTEYTIRVPFKAKWKSPATKKTIVTEGVFKGINSSelkTNYYEVHKT 323
Cdd:cd10140   26 TKTVSVTVTVTVPPGKTVKVTVTVTKAKIDVPYTATLKATYSTSGTGTTGTVSGVFTG---VNYANVETT 92
PFM_parasporin-2-like cd20222
pore-forming module of parasporin-2, hydralysin and similar aerolysin-type beta-barrel ...
 177-288 7.58e-08

pore-forming module of parasporin-2, hydralysin and similar aerolysin-type beta-barrel pore-forming proteins; Bacillus thuringiensis strain A1547 parasporin-2 (PS2, also named Cry46Aa1) is an anti-cancer protein which causes specific cell damage via PS2 oligomerization in the cell membrane. Glycosylphosphatidylinositol (GPI)-anchored proteins may be involved in the cytocidal action of PS2 as co-receptors for PS2's cytocidal action. This family also includes hydralysin (Hln-1) and Hln-2 produced by the green hydra Chlorohydra viridissima. Hydralysin is a paralysis-inducing protein not found in the stinging cells (nematocytes), with a cell type-selective cytolytic activity; it binds erythrocyte membranes and forms discrete pores. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380792  Cd Length: 147  Bit Score: 50.79  E-value: 7.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 177 PVNIHSQEATNDTSEPQTPLIEVLKTTEQqYTFESEVGLELGISTKFSSGIPVAAKAEVKISAKIHTNLSWGIANSHSQT 256
Cdd:cd20222   14 PDILGTTEAVNNGDEEEITVTYSYKVGGK-WTWKTSWSSSSTTGATFSSGIPLEGVFEVGTEFSVSGTTGESGSTSTEKT 92

                         90       100       110
                 ....*....|....*....|....*....|..
gi 627899741 257 WKSSVPLNVPGHKTYKVTMTVTEYTIRVPFKA 288
Cdd:cd20222   93 LTSSVTVKVPPNSKVKITMVTKMKKSSVNYTV 124
PFM_agglutinin-like cd20217
pore-forming module (PFM) of uncharacterized proteins which have agglutatin domain(s), and ...
 177-308 9.20e-08

pore-forming module (PFM) of uncharacterized proteins which have agglutatin domain(s), and similar aerolysin-type beta-barrel pore-forming proteins; Most proteins belonging to this group have an N-terminal agglutatin (also known as amaranthin) lectin domain; some have fascin-like domains which adopt a beta-trefoil topology. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380787 [Multi-domain]  Cd Length: 150  Bit Score: 50.58  E-value: 9.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 177 PVNIHSQEATNDTSEPQTPLIEVLKTTE--QQYTFESEVGLELGISTKFSSGIP--VAAKAEVKISAKIHTNLSWGIANS 252
Cdd:cd20217    1 PLVVGQGSATNNGSEPADMQVQVTLTETvsTSRTWSNSFTFSQSISTTFTAGVPeiASAETTITIGAEQTFGTEWGETTE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 627899741 253 HSQTWKSSVPL-NVPGHKTYKVTMTVTEYTIRVPFKAKWKSPA-----TKKTIVTEGVFKGI 308
Cdd:cd20217   81 EAVQFQSTYLVkDVPPGEEATVTVECSTGKCRVPFTYKTRDTRldgvdRPTVDEIDGVFEGV 142
PFM_tachylectin-like cd20229
pore-forming module (PFM) of uncharacterized proteins having tachylectin domain(s), and ...
 201-313 2.97e-07

pore-forming module (PFM) of uncharacterized proteins having tachylectin domain(s), and similar aerolysin-type beta-barrel pore-forming proteins; Many proteins belonging to this group have tachylectin domain(s), N-terminal to this PFM; some also have an immunoglobulin (Ig) domain. Tachylectins are lectins which bind N-acetylglucosamine and N-acetylgalactosamine. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380799 [Multi-domain]  Cd Length: 148  Bit Score: 49.06  E-value: 2.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 201 KTTEQQYTFESEVGLE--LGISTKFSSGIPVAAKAEVKISAKIHTNLSWGIANSHSQTWKSSVPLN--VPGHKTYKVTMT 276
Cdd:cd20229   26 KTITEVSSFSHSHGFTvaEGAETTFKAGIPVIGEEGIKVILDNSTTHQWNFTTTNEREVTFSLTTNvvVPPGKAVRLEAS 105

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 627899741 277 VTEYTIRVPFKAKWKSPATKKTIVTeGVFKGINSSEL 313
Cdd:cd20229  106 VQKAKIDVPYRAEVITGFGYEVTIT-GTWTGVTVYDL 141
PFM_ABFB-like cd20238
pore-forming module (PFM) of uncharacterized proteins which have an N-terminal ABFB ...
 183-310 3.48e-06

pore-forming module (PFM) of uncharacterized proteins which have an N-terminal ABFB (alpha-L-arabinofuranosidase B) domain, and similar aerolysin-type beta-barrel pore-forming proteins; Most proteins belonging to this group have a PFM C-terminal to an ABFB domain. Alpha-L-arabinofuranosidase (Araf-ase, EC 3.2.1.55) belongs to the glycosyl hydrolase family GH54, and in Aspergillus niger exhibits both Araf-ase, (EC 3.2.1.55) and alpha-D-galactofuranose (Galf-ase) activities, with Galf-ase being less than Araf-ase. Some members have a Ricin-type carbohydrate-binding domain which adopts a beta-trefoil fold. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380808 [Multi-domain]  Cd Length: 146  Bit Score: 46.07  E-value: 3.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 183 QEATNDTSEPQTPLI----EVLKTTEQQYTFESEVGLELGISTKFSSGIP-VAAKAEVKISAKIHTNLSWGIANSHSQTW 257
Cdd:cd20238    6 QDTLIDNSQGSQQMIqfngEISNTNTESYERTDGFELTIGESYTVKASAIiVDEEGQIFFESKTIRNVTYGNQNTTTKTF 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 627899741 258 KSSVPLNVPGHKTYKVTMTVTEYTIRVPFKAKWKSPATKKTIVTEGVFKGINS 310
Cdd:cd20238   86 AYETPLIVPGFSTYNATVIVKSMLLRIPFVATVHFEGLTWVTFFRGVYKGVQS 138
Aerolysin pfam01117
Aerolysin toxin; This family represents the pore forming lobe of aerolysin.
 151-289 3.54e-04

Aerolysin toxin; This family represents the pore forming lobe of aerolysin.


Pssm-ID: 366474  Cd Length: 359  Bit Score: 41.86  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741  151 FTFEAEPLELIniefdLKNTVTESVRPVNIHSQEATNDTSEPQTPLIEVLKTTEQQYTFESEVGLELGISTKFSSGIPva 230
Cdd:pfam01117  80 FKFGVKPSSLK-----YGDPVISDREPYKYIVGYARNDSDTPQQRVLTLSYDEVTNWSKTDTYKYSEKVTIKNKYKFP-- 152

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 627899741  231 AKAEVKISAKIHTNLSWGIANSHSQTW--KSSVPLNVPGHKTYKVTMTVTEYTIRVPFKAK 289
Cdd:pfam01117 153 LIGETELSLELGANQSWATTNGNSSTKtiSDVARVLVPANTKIPVRLKLEKARVDYPYEFN 213
PFM_jacalin-like cd20231
pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin ...
 177-316 1.28e-03

pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin domain, and similar aerolysin-type beta-barrel pore-forming proteins; Jacalin-like lectins are sugar-binding protein domains. Proteins having these lectin domains may bind mono- or oligosaccharides with high specificity. Generally, pore-forming proteins (PFPs) are secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores detrimental to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel. Many of this family are bacterial toxins. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380801 [Multi-domain]  Cd Length: 150  Bit Score: 38.49  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 177 PVNIHSQEATNDTSEPQTPL-IEVLKTTEQQYTFESEVGLELGISTKFSSGIPvaakaevKISAKIHTNLSWGIAN--SH 253
Cdd:cd20231    4 PVTLDSFLPTNNSTDYTWTFsGSRTKTTSRTWSQSSTSGFELSVSVSVSAGIP-------EIGEAVTTSAGWSLSAtsSE 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 627899741 254 SQTWKSSVPL------NVPGHKTYKVTMTVTEYTIRVPFKA----------KWKSPATkktivteGVFKGINSSELKTN 316
Cdd:cd20231   77 SETETTTDELgwsvsgTLPPGEGVKCRATAQEGKLDSDYTStvtvtlqdgeTFSFPEP-------GTFKGVGYSEVDVV 148
PFM_Cry51Aa-like cd20226
pore-forming module of Bacillus thuringiensis insecticidal Cry51A toxin, Bacillus ...
 161-285 4.01e-03

pore-forming module of Bacillus thuringiensis insecticidal Cry51A toxin, Bacillus thuringiensis cytotoxic parasporin-5 and similar aerolysin-type beta-barrel pore-forming proteins; Bacillus thuringiensis parasporin-5 has strong cytocidal activity against several types of cancer cells and may or may not have insecticidal activity. Cry51A toxin is toxic to coleopteran (beetle) larvae. Other members of this family include Bacillus thuringiensis Cry15Aa which is toxic to lepidopteran (butterflies and moth) larvae. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380796 [Multi-domain]  Cd Length: 172  Bit Score: 37.64  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 627899741 161 INIEFDLKNTVTESVRPVNIHS--QEATNDTSEPQTPLIEVLKTTEQQYTFESEVGLELGISTKFSSGIPVA-------- 230
Cdd:cd20226    3 VSNLVAIPPDTIFNVTPGLTFSarQVITNNTSVPQSQTVSFSEKTTETTSTTTTEGYKIGTSIKSTTKFKVKfgfvvgge 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 627899741 231 AKAEVKISAKIHTNLSWGIANSHSQTWKSSVPLNVPGHKTYKVTMTVTEYTIRVP 285
Cdd:cd20226   83 QSIEVSVSFEYNYSTTTTYTTTTEKLWEDTQPVTVPPRTKVTATLIIYGGPFNVP 137
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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